On the role of aromatic side chains in the photoactivation of BLUF domains

M.L. Gauden; J.S. Grinstead; W. Laan; H.M. van Stokkum; M. Avila-Perez; K.C. Toh; R. Boelens; R. Kaptein; R. van Grondelle; K.J. Hellingwerf; J.T.M. Kennis

doi:10.1021/bi7006433

On the role of aromatic side chains in the photoactivation of BLUF domains

M.L. Gauden, J.S. Grinstead, W. Laan, H.M. van Stokkum, M. Avila-Perez, K.C. Toh, R. Boelens, R. Kaptein, R. van Grondelle, K.J. Hellingwerf, J.T.M. Kennis

Biophysics Photosynthesis/Energy

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

BLUF (blue-light sensing using FAD) domain proteins are a novel group of blue-light sensing receptors found in many microorganisms. The role of the aromatic side chains Y21 and W104, which are in close vicinity to the FAD cofactor in the AppA BLUF domain from Rhodobacter sphaeroides, is investigated through the introduction of several amino acid substitutions at these positions. NMR spectroscopy indicated that in the W104F mutant, the local structure of the FAD binding pocket was not significantly perturbed as compared to that of the wild type. Time-resolved fluorescence and absorption spectroscopy was applied to explore the role of Y21 and W104 in AppA BLUF photochemistry. In the Y21 mutants, FADH

Original language	English
Pages (from-to)	7405-7415
Journal	Biochemistry
Volume	46
Issue number	25
DOIs	https://doi.org/10.1021/bi7006433
Publication status	Published - 2007

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On the role of aromatic side chains in the photoactivation of BLUF domains

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title = "On the role of aromatic side chains in the photoactivation of BLUF domains",

abstract = "BLUF (blue-light sensing using FAD) domain proteins are a novel group of blue-light sensing receptors found in many microorganisms. The role of the aromatic side chains Y21 and W104, which are in close vicinity to the FAD cofactor in the AppA BLUF domain from Rhodobacter sphaeroides, is investigated through the introduction of several amino acid substitutions at these positions. NMR spectroscopy indicated that in the W104F mutant, the local structure of the FAD binding pocket was not significantly perturbed as compared to that of the wild type. Time-resolved fluorescence and absorption spectroscopy was applied to explore the role of Y21 and W104 in AppA BLUF photochemistry. In the Y21 mutants, FADH",

author = "M.L. Gauden and J.S. Grinstead and W. Laan and {van Stokkum}, H.M. and M. Avila-Perez and K.C. Toh and R. Boelens and R. Kaptein and {van Grondelle}, R. and K.J. Hellingwerf and J.T.M. Kennis",

note = "On the role of aromatic side chains in the photoactivation of BLUF domains",

year = "2007",

doi = "10.1021/bi7006433",

language = "English",

volume = "46",

pages = "7405--7415",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

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TY - JOUR

T1 - On the role of aromatic side chains in the photoactivation of BLUF domains

AU - Gauden, M.L.

AU - Grinstead, J.S.

AU - Laan, W.

AU - van Stokkum, H.M.

AU - Avila-Perez, M.

AU - Toh, K.C.

AU - Boelens, R.

AU - Kaptein, R.

AU - van Grondelle, R.

AU - Hellingwerf, K.J.

AU - Kennis, J.T.M.

N1 - On the role of aromatic side chains in the photoactivation of BLUF domains

PY - 2007

Y1 - 2007

N2 - BLUF (blue-light sensing using FAD) domain proteins are a novel group of blue-light sensing receptors found in many microorganisms. The role of the aromatic side chains Y21 and W104, which are in close vicinity to the FAD cofactor in the AppA BLUF domain from Rhodobacter sphaeroides, is investigated through the introduction of several amino acid substitutions at these positions. NMR spectroscopy indicated that in the W104F mutant, the local structure of the FAD binding pocket was not significantly perturbed as compared to that of the wild type. Time-resolved fluorescence and absorption spectroscopy was applied to explore the role of Y21 and W104 in AppA BLUF photochemistry. In the Y21 mutants, FADH

AB - BLUF (blue-light sensing using FAD) domain proteins are a novel group of blue-light sensing receptors found in many microorganisms. The role of the aromatic side chains Y21 and W104, which are in close vicinity to the FAD cofactor in the AppA BLUF domain from Rhodobacter sphaeroides, is investigated through the introduction of several amino acid substitutions at these positions. NMR spectroscopy indicated that in the W104F mutant, the local structure of the FAD binding pocket was not significantly perturbed as compared to that of the wild type. Time-resolved fluorescence and absorption spectroscopy was applied to explore the role of Y21 and W104 in AppA BLUF photochemistry. In the Y21 mutants, FADH

U2 - 10.1021/bi7006433

DO - 10.1021/bi7006433

M3 - Article

VL - 46

SP - 7405

EP - 7415

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 25

ER -

On the role of aromatic side chains in the photoactivation of BLUF domains

Abstract

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